Literature summary for 1.8.1.9 extracted from

Cejudo, F.J.; Gonzalez, M.C.; Perez-Ruiz, J.M.
Redox regulation of chloroplast metabolism (2021), Plant Physiol., 186, 9-21 .

Search for more literature for 1.8.1.9

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
chloroplast	-	Arabidopsis thaliana	9507	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
thioredoxin + NADP+	Arabidopsis thaliana	-	thioredoxin disulfide + NADPH + H+	-	r

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	O22229	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
thioredoxin + NADP+	-	Arabidopsis thaliana	thioredoxin disulfide + NADPH + H+	-	r

Subunits

Subunits	Comment	Organism
homodimer	NTRC can be considered as a TRX that bears its own NTR, the catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
NADPH-dependent TRX reductase	-	Arabidopsis thaliana
NTR	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Arabidopsis thaliana
NADPH	-	Arabidopsis thaliana

General Information

General Information	Comment	Organism
malfunction	truncated polypeptides containing either the NTR or the TRX domain of NTRC showed that this novel enzyme could display both activities. Overexpression of 2-Cys PRXs, which has no significant effect in wild-type plants, resultes in further growth impairment in the ntrc mutant background (lacking individual TRXs), showing that the severity of the ntrc phenotype depends on 2-Cys PRXs levels. Very severe growth inhibition phenotypes of mutants combining the deficiencies of NTRC and TRXs f or x are also rescued by decreasing the contents of 2-Cys PRXs	Arabidopsis thaliana
metabolism	regulation of enzyme activity based on thiol-disulfide exchange is a regulatory mechanism in which the protein disulfide reductase activity of thioredoxins (TRXs) plays a central role. Plant chloroplasts are equipped with a complex set of up to 20 TRXs and TRX-like proteins, the activity of which is supported by reducing power provided by photosynthetically reduced ferredoxin (FDX) with the participation of a FDX-dependent TRX reductase (FTR). Therefore, the FDX-FTR-TRXs pathway allows the regulation of redox-sensitive chloroplast enzymes in response to light. In addition, chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. The NTRC gene encodes a polypeptide containing both NTR and TRX domains. NTRC is unique to oxygenic photosynthetic organisms. Both redox systems, NTRC and FDX-FTR-TRXs, participate in fine-tuning chloroplast performance in response to changes in light intensity. Participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control of the reducing activity of chloroplast TRXs as well as in the rapid oxidation of stromal enzymes upon darkness. Analysis of relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems for fine-tuning chloroplast performance in response to changes in light intensity and darkness, overview. The activity of thiol-dependent peroxidases (TPXs) relies on the disulfide reductase activity of NTRC, TRXs, and glutaredoxins (GRXs)	Arabidopsis thaliana
additional information	NTRC can be considered as a TRX that bears its own NTR, which might explain the high catalytic efficiency of the enzyme. The catalytically active form of NTRC is a homodimer arranged in a head-to-tail conformation, which interacts with 2-Cys PRXs through the TRX domain with high affinity for NADPH	Arabidopsis thaliana
physiological function	chloroplasts contain an NADPH-dependent redox system, termed NTRC, which allows the use of NADPH in the redox network of these organelles. Redox regulation is an additional layer of control of the signaling function of the chloroplast. Redox regulation based on dithiol-disulfide interchange constitutes an essential regulatory mechanism that allows the rapid adaptation of chloroplast metabolism to light	Arabidopsis thaliana

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Release 2023.1 (January 2023)